TNFAIP3 Positive Control for STJ500013 peptide (STJ503616)

SPECIFICATIONS
STJ503616-5
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General Information

Short DescriptionTNFAIP3 Positive Control for STJ500013 is synthetically produced from the sequence and is suitable for use in western blot applications.
ApplicationsWB
NoteSTRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.

Product Properties

FormulationProvided as 100 uL ready-to-use, in SDS-PAGE sample buffer (Laemelli's buffer) containing Tris, pH 6.8, 1 % SDS, Glycerol and Bromophenolblue blue as tracking dye. The sample is reduced by adding 2% beta mercaptoethanol. The protein concentration is
Storage InstructionStore at-20°C for long term storage. Avoid freeze-thaw cycles.

Target Information

Gene SymbolTNFAIP3
Gene ID7128
Uniprot IDTNAP3_HUMAN
SpecificityThis is positive control is recommended for use in combination with TNFAIP3 antibody STJ500013.

Additional Info

Post Translational Modifications Proteolytically cleaved by MALT1 upon TCR stimulation.disrupts NF-kappa-B inhibitory function and results in increased IL-2 production. It is proposed that only a fraction of TNFAIP3 colocalized with TCR and CBM complex is cleaved, leaving the main TNFAIP3 pool intact.
Function Ubiquitin-editing enzyme that contains both ubiquitin ligase and deubiquitinase activities. Involved in immune and inflammatory responses signaled by cytokines, such as TNF-alpha and IL-1 beta, or pathogens via Toll-like receptors (TLRs) through terminating NF-kappa-B activity. Essential component of a ubiquitin-editing protein complex, comprising also RNF11, ITCH and TAX1BP1, that ensures the transient nature of inflammatory signaling pathways. In cooperation with TAX1BP1 promotes disassembly of E2-E3 ubiquitin protein ligase complexes in IL-1R and TNFR-1 pathways.affected are at least E3 ligases TRAF6, TRAF2 and BIRC2, and E2 ubiquitin-conjugating enzymes UBE2N and UBE2D3. In cooperation with TAX1BP1 promotes ubiquitination of UBE2N and proteasomal degradation of UBE2N and UBE2D3. Upon TNF stimulation, deubiquitinates 'Lys-63'-polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NF-kappa-B. Deubiquitinates TRAF6 probably acting on 'Lys-63'-linked polyubiquitin. Upon T-cell receptor (TCR)-mediated T-cell activation, deubiquitinates 'Lys-63'-polyubiquitin chains on MALT1 thereby mediating disassociation of the CBM (CARD11:BCL10:MALT1) and IKK complexes and preventing sustained IKK activation. Deubiquitinates NEMO/IKBKG.the function is facilitated by TNIP1 and leads to inhibition of NF-kappa-B activation. Upon stimulation by bacterial peptidoglycans, probably deubiquitinates RIPK2. Can also inhibit I-kappa-B-kinase (IKK) through a non-catalytic mechanism which involves polyubiquitin.polyubiquitin promotes association with IKBKG and prevents IKK MAP3K7-mediated phosphorylation. Targets TRAF2 for lysosomal degradation. In vitro able to deubiquitinate 'Lys-11'-, 'Lys-48'- and 'Lys-63' polyubiquitin chains. Inhibitor of programmed cell death. Has a role in the function of the lymphoid system. Required for LPS-induced production of pro-inflammatory cytokines and IFN beta in LPS-tolerized macrophages.
Peptide Name Tumor Necrosis Factor Alpha-Induced Protein 3
Tnf Alpha-Induced Protein 3
Otu Domain-Containing Protein 7c
Putative Dna-Binding Protein A20
Zinc Finger Protein A20 Cleaved Into - A20p50 - A20p37
Database Links Reactome: R-HSA-168638
Reactome: R-HSA-5357786
Reactome: R-HSA-5357905
Reactome: R-HSA-5357956
Reactome: R-HSA-5689896
Reactome: R-HSA-936440
Cellular Localisation Cytoplasm
Nucleus
Lysosome
A20p50: Cytoplasm
Alternative Peptide Names Tumor Necrosis Factor Alpha-Induced Protein 3 protein
Tnf Alpha-Induced Protein 3 protein
Otu Domain-Containing Protein 7c protein
Putative Dna-Binding Protein A20 protein
Zinc Finger Protein A20 Cleaved Into - A20p50 - A20p37 protein
TNFAIP3 protein
OTUD7C protein

Information sourced from Uniprot.org

Citations

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